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Literature summary extracted from

  • Karuppiah, V.; Thistlethwaite, A.; Dajani, R.; Warwicker, J.; Derrick, J.P.
    Structure and mechanism of the bifunctional CinA enzyme from Thermus thermophilus (2014), J. Biol. Chem., 289, 33187-33197.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.42 gene cinA, recombinant expression of His6-tagged enzyme with a thrombin cleavage site at the N terminus in Escherichia coli strain T7 Thermus thermophilus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.1.42 purified recombinant detagged enzyme free or in complex with nicotinate mononucleotide, or AMP/Mg2+, or ATP/Mg2+, or ribose-ADP/Mg2+, sitting drop vapor diffusion, mixing of 200 nl of protein with 200 nl of well solution containing 0.2 M Na2SO4, 0.1 M Bis-Tris propane, pH 6.5, and 20% w/v, PEG 3350 at 20°C, rodlike crystals, 5-7 days, X-ray diffraction structure determination and analysis at 1.98-2.46 A resolution, molecular replacement and modeling Thermus thermophilus
3.6.1.13 to 2.16 A resolution. The crystal structure shows an unusual asymmetric dimer, with three domains for each chain. The C-terminal domain harbors the nicotinamide mononucleotide deamidase activity. The N-terminal domain belongs to the COG1058 family and is associated with the ADP-ribose diphosphatase activity. The mechanism for the ADP-ribose diphosphatase reaction involves a rotation of the COG1058 domain dimer as part of the reaction cycle Thermus thermophilus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.42 beta-nicotinamide D-ribonucleotide + H2O Thermus thermophilus
-
 beta-nicotinate D-ribonucleotide + NH3
-
 ?
3.5.1.42 beta-nicotinamide D-ribonucleotide + H2O Thermus thermophilus DSM 579
-
 beta-nicotinate D-ribonucleotide + NH3
-
 ?
3.5.1.42 beta-nicotinamide D-ribonucleotide + H2O Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
 beta-nicotinate D-ribonucleotide + NH3
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.42 Thermus thermophilus Q5SHB0 gene cinA
-
3.5.1.42 Thermus thermophilus HB8 / ATCC 27634 / DSM 579 Q5SHB0 gene cinA
-
3.6.1.13 Thermus thermophilus Q5SHB0 enzyme displays both nicotinamide mononucleotide deamidase and ADP-ribose diphosphatase activities
-
3.6.1.13 Thermus thermophilus DSM 579 Q5SHB0 enzyme displays both nicotinamide mononucleotide deamidase and ADP-ribose diphosphatase activities
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.42 recombinant His6-tagged enzyme from Escherichia coli strain T7 by nickel affinity chromatgraphy, cleavage of the tag by thrombin, anion exchange chromatography, and gel filtration Thermus thermophilus

Reaction

EC Number Reaction Comment Organism Reaction ID
3.5.1.42 beta-nicotinamide D-ribonucleotide + H2O = beta-nicotinate D-ribonucleotide + NH3 catalytic mechanism, overview Thermus thermophilus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.42 beta-nicotinamide D-ribonucleotide + H2O
-
 Thermus thermophilus beta-nicotinate D-ribonucleotide + NH3
-
 ?
3.5.1.42 beta-nicotinamide D-ribonucleotide + H2O
-
 Thermus thermophilus DSM 579 beta-nicotinate D-ribonucleotide + NH3
-
 ?
3.5.1.42 beta-nicotinamide D-ribonucleotide + H2O
-
 Thermus thermophilus HB8 / ATCC 27634 / DSM 579 beta-nicotinate D-ribonucleotide + NH3
-
 ?
3.5.1.42 additional information CinA is a bifunctional enzyme exhibiting both nicotinamide mononucleotide deamidase and ADP-ribose diphosphatase activities, ligand binding structures and catalytic mechanism analysis for both activities, overview Thermus thermophilus ?
-
 ?
3.5.1.42 additional information CinA is a bifunctional enzyme exhibiting both nicotinamide mononucleotide deamidase and ADP-ribose diphosphatase activities, ligand binding structures and catalytic mechanism analysis for both activities, overview Thermus thermophilus DSM 579 ?
-
 ?
3.5.1.42 additional information CinA is a bifunctional enzyme exhibiting both nicotinamide mononucleotide deamidase and ADP-ribose diphosphatase activities, ligand binding structures and catalytic mechanism analysis for both activities, overview Thermus thermophilus HB8 / ATCC 27634 / DSM 579 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.1.42 dimer an unusual asymmetric dimer, with three domains for each chain, the C-terminal domain harbors the nicotinamide mononucleotide deamidase activity. The asymmetry in the CinA dimer arises from two alternative orientations of the N-terminal COG1058 domains, only one of which forms a contact with the KH-type domain from the other chain, effectively closing the active site into, we propose, a catalytically competent state Thermus thermophilus

Synonyms

EC Number Synonyms Comment Organism
3.5.1.42 CinA
-
 Thermus thermophilus
3.6.1.13 CinA
-
 Thermus thermophilus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.1.42 37
-
 assay at Thermus thermophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.42 8
-
 assay at Thermus thermophilus

General Information

EC Number General Information Comment Organism
3.5.1.42 evolution the enzyme's N-terminal domain belongs to the COG1058 family and is associated with the ADP-ribose pyrophosphatase activity Thermus thermophilus
3.5.1.42 metabolism the enzyme is associated with natural competence and is proposed to have a function as an enzyme participating in the pyridine nucleotide cycle, which recycles products formed by non-redox uses of NAD+ Thermus thermophilus